Abstract

A mixture of half-molecules of tRNA Phe from yeast, produced by chemical cleavage of the anticodon loop, was isolated by gel filtration on Sephadex G-100 at 57° and fractionated by column chromatography on benzoylated DEAE-cellulose at the same temperature. Rechromatography under identical conditions yielded two major and a minor form of the 3′-half-molecule and a major and a minor form of the 5′ half-molecule. No pronounced differences were found in the amino acid acceptor activities of all complementary fragment combinations.

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